|
Name |
Accession |
Description |
Interval |
E-value |
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
48-329 |
2.30e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 60.72 E-value: 2.30e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770978 48 ATLYRRQNIGSEVET--STIEKQRKELQLLIGELKDRDKELNDMVAVHQRQLLSWEEDRQKVLTLEERCSKLEGELHKRT 125
Cdd:COG1196 229 LLLLKLRELEAELEEleAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLE 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770978 126 DIIKSLMKKVKTLESNQAECQTALQKTQQQLQEMAQKATHSTLLSEDLEARNENLSSTLVDLSAQVGQLQAREQALTTMI 205
Cdd:COG1196 309 ERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEEL 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770978 206 KLKDKDIIEAVNHISDcsgkfklLEHALRDAKMAETCVVREKQDYKQKLKALRIEVNKLKEDLNEKTTENNEQREEIIRL 285
Cdd:COG1196 389 LEALRAAAELAAQLEE-------LEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEAL 461
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1039770978 286 KQEKSCLHDELIFTVEREKRKDELLDIAKSKQDRTNSELQNLRQ 329
Cdd:COG1196 462 LELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEG 505
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
66-329 |
4.62e-09 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 59.69 E-value: 4.62e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770978 66 EKQRKELQLLIGELKDRDKEL----------NDMVAVHQRQL----LSWEEDRQKVLTLEERCSKLEGELHKRTDIIKSL 131
Cdd:TIGR02168 221 ELRELELALLVLRLEELREELeelqeelkeaEEELEELTAELqeleEKLEELRLEVSELEEEIEELQKELYALANEISRL 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770978 132 MKKVKTLESNQAECQTALQKTQQQLQEMAQKATHSTLLSEDLEARNENLSSTLVDLSAQVGQLQAREQALTTMIKLKDKD 211
Cdd:TIGR02168 301 EQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQ 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770978 212 IIEAvnhisdcSGKFKLLEHALRDAKMAETCVVREKQDYKQKLKALRIEVNKLKEDLNEKttENNEQREEIIRLKQEKSC 291
Cdd:TIGR02168 381 LETL-------RSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEA--ELKELQAELEELEEELEE 451
|
250 260 270
....*....|....*....|....*....|....*...
gi 1039770978 292 LHDELIFTVEREKRKDELLDIAKSKQDRTNSELQNLRQ 329
Cdd:TIGR02168 452 LQEELERLEEALEELREELEEAEQALDAAERELAQLQA 489
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
52-329 |
2.30e-08 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 57.39 E-value: 2.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770978 52 RRQNIGSEVETSTIEKQRKELQLLIGELKDRDKELNDMVAVHQRQLLSWEEDRQkvLTLEERCSKLEGELHKRTDIIKSL 131
Cdd:TIGR02169 236 ERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQ--LRVKEKIGELEAEIASLERSIAEK 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770978 132 MKKVKTLESNQAECQTALQKTQQQLQEMAQKATHSTLLSEDLEARNENLSSTLVDLSAQVGQLQAREQALTTMIKLKDKD 211
Cdd:TIGR02169 314 ERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREK 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770978 212 IIEAVNHISDCSGKFKLLEHALRDAKMaetcvvrEKQDYKQKLKALRIEVNKLKEDLNEKTTENNEQREEIIRLKQeksc 291
Cdd:TIGR02169 394 LEKLKREINELKRELDRLQEELQRLSE-------ELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAA---- 462
|
250 260 270
....*....|....*....|....*....|....*...
gi 1039770978 292 lhdeliftvEREKRKDELLDIaKSKQDRTNSELQNLRQ 329
Cdd:TIGR02169 463 ---------DLSKYEQELYDL-KEEYDRVEKELSKLQR 490
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
33-288 |
4.04e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 56.60 E-value: 4.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770978 33 HQLSLGAGESSMNPSATLYRRQNIGSEVETstIEKQRKELQLLIGELKDRDKELNDMVAVHQRQLLSWEEDRQKV----- 107
Cdd:TIGR02168 715 EQLRKELEELSRQISALRKDLARLEAEVEQ--LEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELeaqie 792
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770978 108 ------LTLEERCSKLEGELHKRTDIIKSLMKKVKTLESNQAECQTALQKTQQQLQEMAQKATHSTLLSEDLEARNENLS 181
Cdd:TIGR02168 793 qlkeelKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELE 872
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770978 182 STLVDLSAQVGQLQAREQALTTMIKLKDKDIIEAVNHISDCSGKFKLLEHALRDAKMAETcvvREKQDYKQKLKALRIEV 261
Cdd:TIGR02168 873 SELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLE---GLEVRIDNLQERLSEEY 949
|
250 260 270
....*....|....*....|....*....|.
gi 1039770978 262 NKLKEDL----NEKTTENNEQREEIIRLKQE 288
Cdd:TIGR02168 950 SLTLEEAealeNKIEDDEEEARRRLKRLENK 980
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
62-316 |
5.04e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 52.46 E-value: 5.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770978 62 TSTIEKQRKELQLLIGELKDRDKELNDMVAVHQRQLLSWEEDRQKVLTLEERCSKLEGELHKRTDIIKSLMKKVKTLESN 141
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770978 142 QAECQTALQKTQQQLQEMAQKATHSTLLS----EDLEARNENLSSTLVDLSAQVGQLQAREQALTTmiklkdkdiieavn 217
Cdd:COG4942 99 LEAQKEELAELLRALYRLGRQPPLALLLSpedfLDAVRRLQYLKYLAPARREQAEELRADLAELAA-------------- 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770978 218 hisdcsgkfklLEHALRDAKMAETCVVREKQDYKQKLKALRIEVNKLKEDLNEKTTENNEQREEIIRLKQEKSCLHDELI 297
Cdd:COG4942 165 -----------LRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLE 233
|
250
....*....|....*....
gi 1039770978 298 FTVEREKRKDELLDIAKSK 316
Cdd:COG4942 234 AEAAAAAERTPAAGFAALK 252
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
96-329 |
7.48e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 51.69 E-value: 7.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770978 96 QLLSWEEDRQKVLTLEERCSKLEGELHKRTDIIKSLMKKVKTLESNQAECQTALQKTQQQLQEMAQKAthsTLLSEDLEA 175
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAEL---AELEKEIAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770978 176 RNENLSSTLVDLSAQVGQLQAREQALTTMIKLKDKDIIEAVNhisdcsgKFKLLEHALR-DAKMAETcvVREKQdykQKL 254
Cdd:COG4942 95 LRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVR-------RLQYLKYLAPaRREQAEE--LRADL---AEL 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039770978 255 KALRIEVNKLKEDLNEKTTENNEQREEIIRLKQEKSCLHDELiftVEREKRKDELLDIAKSKQDRTNSELQNLRQ 329
Cdd:COG4942 163 AALRAELEAERAELEALLAELEEERAALEALKAERQKLLARL---EKELAELAAELAELQQEAEELEALIARLEA 234
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
125-368 |
1.51e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 51.60 E-value: 1.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770978 125 TDIIKSLMKKVKTLESnQAECQTALQKTQQQLqemaqKATHSTLLSEDLEARNENLSStlvdLSAQVGQLQAREQALTTM 204
Cdd:TIGR02168 192 EDILNELERQLKSLER-QAEKAERYKELKAEL-----RELELALLVLRLEELREELEE----LQEELKEAEEELEELTAE 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770978 205 IKLKDKDIIEAVNHISDCSGKFKLLEHALRDAKMAETCVVREKQDYKQKLKALRIEV--------------NKLKEDLNE 270
Cdd:TIGR02168 262 LQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLeeleaqleelesklDELAEELAE 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770978 271 KTTENNEQREEIIRLKQEKSCLHDELIFTVEREKRKDELLDIAKSKQDRTNSELQNLRQIYVKQQSDLQFLNFNIESSQE 350
Cdd:TIGR02168 342 LEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQ 421
|
250
....*....|....*...
gi 1039770978 351 LIQIHGLKMEEPKALECS 368
Cdd:TIGR02168 422 EIEELLKKLEEAELKELQ 439
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
125-366 |
2.58e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 50.71 E-value: 2.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770978 125 TDIIKSLMKKVKTLEsNQAEcqTALQKTQQQLQEMAQKATHSTLLSEDLEARNENLSSTLVDLSAQVGQLQAREQALTTM 204
Cdd:COG1196 192 EDILGELERQLEPLE-RQAE--KAERYRELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAE 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770978 205 IKLKDKDIIEAVNHISDCSGKFKLLEHALRDAKMAETCVVREKQDYKQKLKALRIEVNKLKEDLNEKTTENNEQREEIIR 284
Cdd:COG1196 269 LEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEE 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770978 285 LKQEKSCLHDELIFTVEREKRKD-ELLDIAKSKQDRTNSELQNLRQIYVKQQSDLQFLNFNIESSQELIQIHGLKMEEPK 363
Cdd:COG1196 349 AEEELEEAEAELAEAEEALLEAEaELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEE 428
|
...
gi 1039770978 364 ALE 366
Cdd:COG1196 429 ALA 431
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
63-353 |
3.08e-06 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 50.40 E-value: 3.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770978 63 STIEKQRKELQLLIGELKDRDKELNDMVAVHQRQLLSWEEDRQKVLTLEERCSKLEGELHKRTDIIKSLMKKVKTLESNQ 142
Cdd:TIGR04523 398 SKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSI 477
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770978 143 AECQTALQKTQQQLQEMAQKatHSTLLSEdlearNENLSSTLVDLSAQVGQLQAREQALTTMIKLKDKDIieavnhiSDC 222
Cdd:TIGR04523 478 NKIKQNLEQKQKELKSKEKE--LKKLNEE-----KKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKI-------SDL 543
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770978 223 SGKFKLLEHALRDAKMAEtcVVREKQ----DYKQKLKALRIEVNKLKEDLNEKTTENNEQREEIIRLKQEKSCLHDELIF 298
Cdd:TIGR04523 544 EDELNKDDFELKKENLEK--EIDEKNkeieELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEK 621
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1039770978 299 TVEREKRKDELLDIAKSKQDRTNSELQNLRQIYVKQQSDLQFLNFNIESSQELIQ 353
Cdd:TIGR04523 622 AKKENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIRNKWPEIIKKIKESKTKID 676
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
72-353 |
4.53e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 49.94 E-value: 4.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770978 72 LQLLIGELKDRDKELNDMVAVHQR--QLLSWEEDRQKVLTLEERcSKLEGELHKRTDIIKSLMKKVKTLESNQAECQTAL 149
Cdd:COG1196 191 LEDILGELERQLEPLERQAEKAERyrELKEELKELEAELLLLKL-RELEAELEELEAELEELEAELEELEAELAELEAEL 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770978 150 QKTQQQLQEmaqkathstlLSEDLEARNENLSS-----------------TLVDLSAQVGQLQAREQALTTMIKLKDKDI 212
Cdd:COG1196 270 EELRLELEE----------LELELEEAQAEEYEllaelarleqdiarleeRRRELEERLEELEEELAELEEELEELEEEL 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770978 213 IEAVNHISDCSGKFKLLEHALRDAKMAETCVVREKQDYKQKLKALRIEVNKLKEDLNEKTTENNEQREEIIRLKQEKSCL 292
Cdd:COG1196 340 EELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERL 419
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039770978 293 HDELIFTVEREKRKDELLDIAKSKQDRTNSELQNLRQIYVKQQSDLQFLNFNIESSQELIQ 353
Cdd:COG1196 420 EEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALA 480
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
65-324 |
2.08e-05 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 47.76 E-value: 2.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770978 65 IEKQRKELQLLIGELKDRDKELNDMvavhqRQLLSWEEdrQKVLTLEERCSKLEGELHKRTDIIKSLMKKVKTLESNQAE 144
Cdd:TIGR02169 683 LEGLKRELSSLQSELRRIENRLDEL-----SQELSDAS--RKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIEN 755
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770978 145 CQTALQKTQQQLQEMAQKATHSTLLSEDLEARN------------ENLSSTLVDLSAQVGQLQAREQALTTMIKLKDKDI 212
Cdd:TIGR02169 756 VKSELKELEARIEELEEDLHKLEEALNDLEARLshsripeiqaelSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEI 835
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770978 213 IEAVNHISDCSGKFKLLEHALRDAKMaetcvvrEKQDYKQKLKALRIEVNKLKEDLNEKTTENNEQREEIIRLKQEKscl 292
Cdd:TIGR02169 836 QELQEQRIDLKEQIKSIEKEIENLNG-------KKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKI--- 905
|
250 260 270
....*....|....*....|....*....|..
gi 1039770978 293 hDELIFTVEREKRKDELLDIAKSKQDRTNSEL 324
Cdd:TIGR02169 906 -EELEAQIEKKRKRLSELKAKLEALEEELSEI 936
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
64-282 |
2.34e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.60 E-value: 2.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770978 64 TIEKQRKELQLLIGELKDRDKELNDmVAVHQRQLLSWEEDRQKVL-------TLEERCSKLEGELHKRTDIIKSLMKKVK 136
Cdd:COG4913 638 AELDALQERREALQRLAEYSWDEID-VASAEREIAELEAELERLDassddlaALEEQLEELEAELEELEEELDELKGEIG 716
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770978 137 TLESNQAECQTALQKTQQQLQEMAQKAthSTLLSEDLEARNENLSSTlvDLSAQVG-QLQAREQALTTMIKLKDKDIIEA 215
Cdd:COG4913 717 RLEKELEQAEEELDELQDRLEAAEDLA--RLELRALLEERFAAALGD--AVERELReNLEERIDALRARLNRAEEELERA 792
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770978 216 VNHISDcsgKFKLLEHALRDAkmaetcvVREKQDYKQKLKALRIE-----VNKLKEDLNEKTTEN--------NEQREEI 282
Cdd:COG4913 793 MRAFNR---EWPAETADLDAD-------LESLPEYLALLDRLEEDglpeyEERFKELLNENSIEFvadllsklRRAIREI 862
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
65-297 |
4.01e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.83 E-value: 4.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770978 65 IEKQRKELQLL--IGELKDRDKELNDMVAVHQ--RQLLSWEEDRQKVLTLEERCSKLEGELhkrtdiikslmkkvKTLES 140
Cdd:COG4913 244 LEDAREQIELLepIRELAERYAAARERLAELEylRAALRLWFAQRRLELLEAELEELRAEL--------------ARLEA 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770978 141 NQAECQTALQKTQQQLQEM-AQKATHSTLLSEDLEARNENLSSTLVDLSAQVGQLQAreqaLTTMIKLKDKDIIEAvnhi 219
Cdd:COG4913 310 ELERLEARLDALREELDELeAQIRGNGGDRLEQLEREIERLERELEERERRRARLEA----LLAALGLPLPASAEE---- 381
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1039770978 220 sdcsgkFKLLEHALRDAKmaetcvvrekQDYKQKLKALRIEVNKLKEDLNEKTTENNEQREEIIRLKQEKSCLHDELI 297
Cdd:COG4913 382 ------FAALRAEAAALL----------EALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLL 443
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
125-353 |
4.14e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 46.30 E-value: 4.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770978 125 TDIIKSLMKKVKTLESNQAECQTALQKTQQQLQEMAQKATHSTLLSEDLEARNENLSSTLVDLSAQVGQLQAREQALTTM 204
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770978 205 IKLKDKDIIEAVNHISDcSGKFKLLEHALRDAKMAETcvVREKQDYKQKLKALRIEVNKLKEDLnekttenneqrEEIIR 284
Cdd:COG4942 99 LEAQKEELAELLRALYR-LGRQPPLALLLSPEDFLDA--VRRLQYLKYLAPARREQAEELRADL-----------AELAA 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1039770978 285 LKQEKSCLHDELIFTVEREKRKDELLDIAKSKQDRTnseLQNLRQIYVKQQSDLQFLNFNIESSQELIQ 353
Cdd:COG4942 165 LRAELEAERAELEALLAELEEERAALEALKAERQKL---LARLEKELAELAAELAELQQEAEELEALIA 230
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
54-360 |
7.46e-05 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 46.17 E-value: 7.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770978 54 QNIGSEVETSTIEKQRKELQLLIGELKDRDKELNDmvavhqrqllsweedrqkvltLEERCSKLEGELHKRTDIIKSLMK 133
Cdd:TIGR04523 291 NQLKSEISDLNNQKEQDWNKELKSELKNQEKKLEE---------------------IQNQISQNNKIISQLNEQISQLKK 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770978 134 KVKTLESNQAECQTALQKTQQQLQEMAQKATHSTLLSEDLEARNENLSSTLVDLSAQVGQLQAREQALTTMIKLKDKDII 213
Cdd:TIGR04523 350 ELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIE 429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770978 214 EAVNHISDCSGKFKLLEHALRDAKMAETCVVREKQDYKQKLKALRIEVNKLKEDLNEKTTENNEQREEIIRLKQEKSCLH 293
Cdd:TIGR04523 430 RLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELE 509
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039770978 294 DELiftVEREKRKDELldiaKSKQDRTNSELQNLRQIYVKQQSDLQFLNFNIESSQELIQIHGLKME 360
Cdd:TIGR04523 510 EKV---KDLTKKISSL----KEKIEKLESEKKEKESKISDLEDELNKDDFELKKENLEKEIDEKNKE 569
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
85-288 |
9.09e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 45.68 E-value: 9.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770978 85 ELNDMVAVHQRQLLSWEeDRQKVLTLEERCSKLEGELHKRTDIIKSLMKKVKTLESNQAECQtALQKTQQQLQEMAQkaT 164
Cdd:COG4913 591 EKDDRRRIRSRYVLGFD-NRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQ-RLAEYSWDEIDVAS--A 666
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770978 165 HSTLlsEDLEARNENLSSTLVDLSA---QVGQLQAREQALTTMIKLKDKDIIEAVNHISDCSGKFKLLEHALRDAkmAET 241
Cdd:COG4913 667 EREI--AELEAELERLDASSDDLAAleeQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAA--EDL 742
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1039770978 242 CVVREKQDYKQKLKALRIE--VNKLKEDLNEK----TTENNEQREEIIRLKQE 288
Cdd:COG4913 743 ARLELRALLEERFAAALGDavERELRENLEERidalRARLNRAEEELERAMRA 795
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
71-378 |
1.34e-04 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 45.49 E-value: 1.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770978 71 ELQLLIGELKDRDKELNdmVAVHQRQLLsWEEDRQKVLTLEErcskLEGELHKRTDIIKSLMKKVKTLESnqaECQTALQ 150
Cdd:pfam15921 378 QLQKLLADLHKREKELS--LEKEQNKRL-WDRDTGNSITIDH----LRRELDDRNMEVQRLEALLKAMKS---ECQGQME 447
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770978 151 KTQQQLQEMAQKATHSTLLSEDLEARNENLSSTLVDLSAQVGQLQAREQA---LTTMIKLKDKdIIEAVN-HISDCSGKF 226
Cdd:pfam15921 448 RQMAAIQGKNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTvsdLTASLQEKER-AIEATNaEITKLRSRV 526
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770978 227 kllehalrDAKMAETCVVREKQDYkqkLKALRIEVNKLKEDLNEKTTENNEQREEIIRLKQ--------------EKSCL 292
Cdd:pfam15921 527 --------DLKLQELQHLKNEGDH---LRNVQTECEALKLQMAEKDKVIEILRQQIENMTQlvgqhgrtagamqvEKAQL 595
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770978 293 HDELiftverEKRKDEL--LDIAKSKQDRTNSELQnlrqiyvKQQSDLQFLNFNI--ESSQELIQIHGLKMEEPKALECS 368
Cdd:pfam15921 596 EKEI------NDRRLELqeFKILKDKKDAKIRELE-------ARVSDLELEKVKLvnAGSERLRAVKDIKQERDQLLNEV 662
|
330
....*....|
gi 1039770978 369 KDmCLSDLDN 378
Cdd:pfam15921 663 KT-SRNELNS 671
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
63-203 |
2.49e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 44.37 E-value: 2.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770978 63 STIEKQRKELQLLIGELKDRDKELNDMVAvHQRQLLSWEEDRQKVLTLEERCSKLEGELHKRTDIIKSLMKKVKTLESNQ 142
Cdd:COG4717 98 EELEEELEELEAELEELREELEKLEKLLQ-LLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQ 176
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039770978 143 AECQTALQK----TQQQLQEMAQKAthstllsEDLEARNENLSSTLVDLSAQVGQLQAREQALTT 203
Cdd:COG4717 177 EELEELLEQlslaTEEELQDLAEEL-------EELQQRLAELEEELEEAQEELEELEEELEQLEN 234
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
84-364 |
3.35e-04 |
|
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.
Pssm-ID: 284517 [Multi-domain] Cd Length: 749 Bit Score: 43.97 E-value: 3.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770978 84 KELNDMVAVHQRQLLSWEEDRQKVL-TLEERCSKLEGELH----KRTDIIKSLMKKVKTLESNQAEcqtaLQKTQQQLQ- 157
Cdd:pfam07111 140 RELEEIQRLHQEQLSSLTQAHEEALsSLTSKAEGLEKSLNsletKRAGEAKQLAEAQKEAELLRKQ----LSKTQEELEa 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770978 158 -----EMAQKATHSTLLSE----DLEARNENLSSTL-------VDLSAQVGQLQAREQALTTMIKLKDKDIIEAVNHISD 221
Cdd:pfam07111 216 qvtlvESLRKYVGEQVPPEvhsqTWELERQELLDTMqhlqedrADLQATVELLQVRVQSLTHMLALQEEELTRKIQPSDS 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770978 222 CSGKF-KLLEHALRD--AKMAETCVVREKQD--YKQKLKALRIEVNKLKedlnEKTTENNEQREEIIRLKQEKSCLhdel 296
Cdd:pfam07111 296 LEPEFpKKCRSLLNRwrEKVFALMVQLKAQDleHRDSVKQLRGQVAELQ----EQVTSQSQEQAILQRALQDKAAE---- 367
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1039770978 297 iFTVEREKRKDELLDIAKSKQDRTNSELQNlrqiyVKQQSDLQFLNFNIESSQELIQIHGLKMEEPKA 364
Cdd:pfam07111 368 -VEVERMSAKGLQMELSRAQEARRRQQQQT-----ASAEEQLKFVVNAMSSTQIWLETTMTRVEQAVA 429
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
65-243 |
6.50e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 42.84 E-value: 6.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770978 65 IEKQRKELQlliGELKDRDKELNDMvavhQRQLLsweedrQKVLTLEERCSKLEGELHKRTDIIKSLMKKVKTLESNQAE 144
Cdd:PRK12704 66 IHKLRNEFE---KELRERRNELQKL----EKRLL------QKEENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEE 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770978 145 CQTALQKTQQQLQEMAQkathstlLSEDlEARNENLSSTLVDLSAQVGQL------QAREQAlttmiKLKDKDIIeaVNH 218
Cdd:PRK12704 133 LEELIEEQLQELERISG-------LTAE-EAKEILLEKVEEEARHEAAVLikeieeEAKEEA-----DKKAKEIL--AQA 197
|
170 180
....*....|....*....|....*
gi 1039770978 219 ISDCSGkfkllEHAlrdakmAETCV 243
Cdd:PRK12704 198 IQRCAA-----DHV------AETTV 211
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
61-329 |
6.80e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 43.11 E-value: 6.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770978 61 ETSTIEKQRKELQLLIGELKDRDKELNDMVAVHQRQLLSWEEDRQKVL------------------TLEERCSKLEGEL- 121
Cdd:PRK02224 252 ELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLaeaglddadaeavearreELEDRDEELRDRLe 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770978 122 HKRTDI------IKSLMKKVKTLESNQAE--------------CQTALQKTQQQLQEMAQKATHSTLLSEDLEARNENLS 181
Cdd:PRK02224 332 ECRVAAqahneeAESLREDADDLEERAEElreeaaeleseleeAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAE 411
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770978 182 STLVDLSAQVGQLQAREQALTTMIKLKDKDIIEA---------------------VNHISDCSGKFKLLEHALRDAKmAE 240
Cdd:PRK02224 412 DFLEELREERDELREREAELEATLRTARERVEEAealleagkcpecgqpvegsphVETIEEDRERVEELEAELEDLE-EE 490
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770978 241 TCVVREKQDYKQKLKALRIEVNKLKED-------LNEKTTENNEQREEIIRLKQEKSCLHDElifTVEREKRKDELLDIA 313
Cdd:PRK02224 491 VEEVEERLERAEDLVEAEDRIERLEERredleelIAERRETIEEKRERAEELRERAAELEAE---AEEKREAAAEAEEEA 567
|
330
....*....|....*....
gi 1039770978 314 KSKQDRT---NSELQNLRQ 329
Cdd:PRK02224 568 EEAREEVaelNSKLAELKE 586
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
65-287 |
6.91e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.83 E-value: 6.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770978 65 IEKQRKEL--------QLLIGELKDRDKELNDMvavhQRQLLSWEEDRQKVLTLEERCSKLEGELHKRTDIIKSLMKKVK 136
Cdd:COG4717 51 LEKEADELfkpqgrkpELNLKELKELEEELKEA----EEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQ 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770978 137 TLESNQaecqtALQKTQQQLQEMAQKAthstllsEDLEARNENLSSTLVDLSAQVGQLQAREQALTTMIKLKDKDIIEAv 216
Cdd:COG4717 127 LLPLYQ-----ELEALEAELAELPERL-------EELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEE- 193
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039770978 217 nhisdcsgkfklLEHALRDAKMAEtcvvREKQDYKQKLKALRIEVNKLKEDLN--EKTTENNEQREEIIRLKQ 287
Cdd:COG4717 194 ------------LQDLAEELEELQ----QRLAELEEELEEAQEELEELEEELEqlENELEAAALEERLKEARL 250
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
52-366 |
7.00e-04 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 43.11 E-value: 7.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770978 52 RRQNIGSEV--ETSTIEKQRKELQLLIGELKDRDKELNDMVAVHQRQLLSWEEDRQkvltLEERCSKLEGELHKRTdiIK 129
Cdd:TIGR00606 752 KLQKVNRDIqrLKNDIEEQETLLGTIMPEEESAKVCLTDVTIMERFQMELKDVERK----IAQQAAKLQGSDLDRT--VQ 825
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770978 130 SLMKKVktlesnqaecqtalQKTQQQLQEMAQKATHSTLLSEDLEARNENLSSTLVDLSA---QVGQLQAREQALTTMIK 206
Cdd:TIGR00606 826 QVNQEK--------------QEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSeklQIGTNLQRRQQFEEQLV 891
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770978 207 LKDKDIIEAVNHISDCSGKFKLLEHALRDAKMAETCVVREKQDYKQKLKalrIEVNKLKEDLNE-----KTTENNEQREE 281
Cdd:TIGR00606 892 ELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQ---DKVNDIKEKVKNihgymKDIENKIQDGK 968
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770978 282 IIRLKQEKSCLHDELIFTVEREKRKDELLDiaKSKQDRTNSELQNLRQIYVKQQSDLQFLNFNIESSQELIQIHGLKMEE 361
Cdd:TIGR00606 969 DDYLKQKETELNTVNAQLEECEKHQEKINE--DMRLMRQDIDTQKIQERWLQDNLTLRKRENELKEVEEELKQHLKEMGQ 1046
|
....*
gi 1039770978 362 PKALE 366
Cdd:TIGR00606 1047 MQVLQ 1051
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
65-366 |
8.39e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 42.20 E-value: 8.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770978 65 IEKQRKELQLLIGELKDRDKELNDMvavhQRQLlswEEDRQKVLTLEERCSKLEGELHKRTDIIKSLMKKVKTLESNQAE 144
Cdd:COG4372 40 LDKLQEELEQLREELEQAREELEQL----EEEL---EQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEE 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770978 145 CQTALQKTQQQLQEMAQKATHSTLLSEDLEARNENLSSTLVDLSAQVGQLQAREQAL-TTMIKLKDKDIIEAVNHISDCS 223
Cdd:COG4372 113 LQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALeQELQALSEAEAEQALDELLKEA 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770978 224 GKFKLLEHALRDAKMAETCVVREKQDYKQKLKALRIEVNKLKEDLNEKTTENNEQREEIIRLKQEKSclhDELIFTVERE 303
Cdd:COG4372 193 NRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKE---IEELELAILV 269
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039770978 304 KRKDELLDIAKSKQDRTNSELQNLRQIYVKQQSDLQFLNFNIESSQELIQIHGLKMEEPKALE 366
Cdd:COG4372 270 EKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELAL 332
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
66-326 |
8.69e-04 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 42.47 E-value: 8.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770978 66 EKQRKELQLLIGELKDRDKELNDMVAVHQRQLLSWEEDRQkvlTLEERCSKLEGELHKRTDIIKSLMKKVKTLESNQAEC 145
Cdd:pfam01576 116 EAARQKLQLEKVTTEAKIKKLEEDILLLEDQNSKLSKERK---LLEERISEFTSNLAEEEEKAKSLSKLKNKHEAMISDL 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770978 146 QTALQKTQQQLQEMAQkathstlLSEDLEARNENLSSTLVDLSAQV----GQLQAREQALTTMI-KLKD---------KD 211
Cdd:pfam01576 193 EERLKKEEKGRQELEK-------AKRKLEGESTDLQEQIAELQAQIaelrAQLAKKEEELQAALaRLEEetaqknnalKK 265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770978 212 IIEAVNHISDcsgkfklLEHALRDAKMAETCVVREKQDYKQKLKALRI---------------------EVNKLKEDLNE 270
Cdd:pfam01576 266 IRELEAQISE-------LQEDLESERAARNKAEKQRRDLGEELEALKTeledtldttaaqqelrskreqEVTELKKALEE 338
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1039770978 271 KTTENNEQREEiirLKQEKSCLHDELIFTVEREKRKDELLDIAKSKQDRTNSELQN 326
Cdd:pfam01576 339 ETRSHEAQLQE---MRQKHTQALEELTEQLEQAKRNKANLEKAKQALESENAELQA 391
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
54-353 |
9.24e-04 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 42.31 E-value: 9.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770978 54 QNIGSEVETSTIEKQRKELQLLIGELKD-RDKELNDMVavhqrqllswEEDRQKVLTLEERCSKLEGELHKRTDIIKSLM 132
Cdd:TIGR04523 183 LNIQKNIDKIKNKLLKLELLLSNLKKKIqKNKSLESQI----------SELKKQNNQLKDNIEKKQQEINEKTTEISNTQ 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770978 133 KKVKTLESNQAECQTALQKTQQQLQemaqkaTHSTLLSEdLEARNENLSSTLVDLSAQVGQLQAREqaLTTMIKLKDKDI 212
Cdd:TIGR04523 253 TQLNQLKDEQNKIKKQLSEKQKELE------QNNKKIKE-LEKQLNQLKSEISDLNNQKEQDWNKE--LKSELKNQEKKL 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770978 213 IEAVNHISDCSGKFKLLEHALRDAKMAET---------------------CVVREKQDYKQKLKALRIEVNKLKEDLNEK 271
Cdd:TIGR04523 324 EEIQNQISQNNKIISQLNEQISQLKKELTnsesensekqreleekqneieKLKKENQSYKQEIKNLESQINDLESKIQNQ 403
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770978 272 TTENNEQREEIIRLKQEKSCLHDEL-IFTVEREKRKDELLDIAKSKQDRTNS--ELQNLRQIYVKQQSDLQFLNFNIESS 348
Cdd:TIGR04523 404 EKLNQQKDEQIKKLQQEKELLEKEIeRLKETIIKNNSEIKDLTNQDSVKELIikNLDNTRESLETQLKVLSRSINKIKQN 483
|
....*
gi 1039770978 349 QELIQ 353
Cdd:TIGR04523 484 LEQKQ 488
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
65-366 |
9.99e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 41.81 E-value: 9.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770978 65 IEKQRKELQLLIGELKDRDKELNDMVAVHQRQLLSWEEDRQKVLTLEERCSKLEGELHKRTDIIKSLMKKVKTLESNQAE 144
Cdd:COG4372 68 LEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAE 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770978 145 CQTALQKTQQQLQEMAQK--ATHSTLLSEDLEARNENLSSTLVDLSAQVGQLQAREQALTTMIKLKDKDIIEAVNHISDC 222
Cdd:COG4372 148 REEELKELEEQLESLQEElaALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSL 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770978 223 SGKFKLLEHALRDAKMAEtcVVREKQDYKQKLKALRIEVNKLKEDLNEKTTENNEQREEIIRLKQEKSCLHDELIFTV-E 301
Cdd:COG4372 228 EAKLGLALSALLDALELE--EDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNlA 305
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039770978 302 REKRKDELLDIAKSKQDRTNSELQNLRQIYVKQQSDLQFLNFNIESSQELIQIHGLKMEEPKALE 366
Cdd:COG4372 306 ALSLIGALEDALLAALLELAKKLELALAILLAELADLLQLLLVGLLDNDVLELLSKGAEAGVADG 370
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
237-365 |
1.99e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 41.30 E-value: 1.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770978 237 KMAETCVVREKQDYKQKLKALRIEVNKLKEdlnEKTTEnneQREEIIRLKQEkscLHDEL------IFTVE-REKRKDEL 309
Cdd:PRK12704 27 KIAEAKIKEAEEEAKRILEEAKKEAEAIKK---EALLE---AKEEIHKLRNE---FEKELrerrneLQKLEkRLLQKEEN 97
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039770978 310 LDIAKSKQDRTNSELQNLRQIYVKQQSDLQFLNFNIESS-----QELIQIHGLKMEEPKAL 365
Cdd:PRK12704 98 LDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELieeqlQELERISGLTAEEAKEI 158
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
51-289 |
2.69e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.82 E-value: 2.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770978 51 YRRQNIGSEVE-TSTIEKQRKELQLLIGELKDRDKELNDM-------VAVHQRQLLSWEEDRQKVLTLEERCSKLEGELH 122
Cdd:PRK03918 176 RRIERLEKFIKrTENIEELIKEKEKELEEVLREINEISSElpelreeLEKLEKEVKELEELKEEIEELEKELESLEGSKR 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770978 123 KRTDIIKSLMKKVKTLESNQAEcqtaLQKTQQQLQEMAQKATHSTLLSEDLEARNE---NLSSTLVDLSAQVGQLQAREQ 199
Cdd:PRK03918 256 KLEEKIRELEERIEELKKEIEE----LEEKVKELKELKEKAEEYIKLSEFYEEYLDelrEIEKRLSRLEEEINGIEERIK 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770978 200 ALTTM---IKLKDKDIIEAVNHISDCSGKFKLLEHA------LRDAKMAETC-----VVREKQDYKQKLKALRIEVNKLK 265
Cdd:PRK03918 332 ELEEKeerLEELKKKLKELEKRLEELEERHELYEEAkakkeeLERLKKRLTGltpekLEKELEELEKAKEEIEEEISKIT 411
|
250 260
....*....|....*....|....
gi 1039770978 266 EDLNEKTTENNEQREEIIRLKQEK 289
Cdd:PRK03918 412 ARIGELKKEIKELKKAIEELKKAK 435
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
70-401 |
2.75e-03 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 40.86 E-value: 2.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770978 70 KELQLLIGELKDRDKELNDMVAVHQrqlLSWEEDRQKVLTLEERCSKLEGELHKRTDIIKSLmkkvkTLEsnqaecqtaL 149
Cdd:pfam05483 324 KTICQLTEEKEAQMEELNKAKAAHS---FVVTEFEATTCSLEELLRTEQQRLEKNEDQLKII-----TME---------L 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770978 150 QKTQQQLQEMAQKATHSTLLSEDLE---ARNENLSSTLVDLSAQVGQLQAREQALTTMIKLKDKDIIEavnhisdcsgkf 226
Cdd:pfam05483 387 QKKSSELEEMTKFKNNKEVELEELKkilAEDEKLLDEKKQFEKIAEELKGKEQELIFLLQAREKEIHD------------ 454
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770978 227 klLEHALRDAKMAETCVVREKQDYKQKLKALRIEVNKLKEDLNEKTTENNEQREEIIRLKQEKSCLHDELIFTVEREKRK 306
Cdd:pfam05483 455 --LEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEERM 532
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770978 307 DELLDIAKSKQDRTNSELQNLRQIYVKQQSDLQFLNFNIESSQELIQIHGLKMEEPKALECSKDMCLSDLDNNYPKIDIK 386
Cdd:pfam05483 533 LKQIENLEEKEMNLRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEE 612
|
330
....*....|....*
gi 1039770978 387 RERNQKSLVKDQTFE 401
Cdd:pfam05483 613 LHQENKALKKKGSAE 627
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
51-418 |
3.05e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 40.80 E-value: 3.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770978 51 YRRQNIGSEVETSTIEKQRKELQLLIGELKDRDKELNDMVAVHQRQLLSWEEDRQKV-----LTLEERCSKLEGELHKRT 125
Cdd:TIGR00606 317 KERELVDCQRELEKLNKERRLLNQEKTELLVEQGRLQLQADRHQEHIRARDSLIQSLatrleLDGFERGPFSERQIKNFH 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770978 126 DIIKSLMK-KVKTLESNQAECQTALQKTQQQLQEMAQKATHstlLSEDLEARNENLSSTLVDLSAQVGQLQAREQALTTM 204
Cdd:TIGR00606 397 TLVIERQEdEAKTAAQLCADLQSKERLKQEQADEIRDEKKG---LGRTIELKKEILEKKQEELKFVIKELQQLEGSSDRI 473
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770978 205 IKlKDKDIIEAVNHISdcsgkfKLLEHALRDAKMAETCVVR-EKQDYKQKLKAL---RIEVNKLKEDLNEKTTENNEQRE 280
Cdd:TIGR00606 474 LE-LDQELRKAERELS------KAEKNSLTETLKKEVKSLQnEKADLDRKLRKLdqeMEQLNHHTTTRTQMEMLTKDKMD 546
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770978 281 EIIRLKQEKSCLHDELIFTVEREKRKDELLDIAKSKQDRTNSELQNLRQIYVKQQSDLQFLNfNIESSQELIQIHGLKME 360
Cdd:TIGR00606 547 KDEQIRKIKSRHSDELTSLLGYFPNKKQLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKN-HINNELESKEEQLSSYE 625
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770978 361 EPKALECSKDMCLSDLDNnyPKIDIKRERNQKSLVKDQT--FEVMLAQHNGSDKSSCDAC 418
Cdd:TIGR00606 626 DKLFDVCGSQDEESDLER--LKEEIEKSSKQRAMLAGATavYSQFITQLTDENQSCCPVC 683
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
52-396 |
3.56e-03 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 40.73 E-value: 3.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770978 52 RRQNIGSEVETSTIEKQRKELQLLIGELKDRDKELNDMVAVHQRQLLSWEEDRQKVLTLEERCSKLEGELHKRTdiiksL 131
Cdd:pfam02463 154 RRLEIEEEAAGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLL-----Y 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770978 132 MKKVKTLESNQAECQTALQKTQQQLQEMAQKathstllsEDLEARNENLSSTLVDLSAQVGQLQAREQALTTMIKLKDKD 211
Cdd:pfam02463 229 LDYLKLNEERIDLLQELLRDEQEEIESSKQE--------IEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKS 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770978 212 IIEavnhisdcsgKFKLLEHALRDAKMAETCVVREKQDYKQKLKALRIEVNKLKEDLNEKTTENNEQREEIIRLKQEKSC 291
Cdd:pfam02463 301 ELL----------KLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQ 370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770978 292 LHDELIFTV----EREKRKDELLDIAKSKQDRTNSELQNLRQIYVKQQSDLQFLNFNIESSQELIQIHGLKMEEPKALEC 367
Cdd:pfam02463 371 LEEELLAKKklesERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEK 450
|
330 340
....*....|....*....|....*....
gi 1039770978 368 SKDMCLSDLDNNYPKIDIKRERNQKSLVK 396
Cdd:pfam02463 451 EELEKQELKLLKDELELKKSEDLLKETQL 479
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
138-354 |
3.62e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 40.39 E-value: 3.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770978 138 LESNQAECQTALQKTQQQLQEMAQKatHSTLlseDLEARNENLSSTLVDLSAQVGQLQAREQALTTMIKLKDKDIIEAVN 217
Cdd:COG3206 180 LEEQLPELRKELEEAEAALEEFRQK--NGLV---DLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPD 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770978 218 HISDcsgkfkllehALRDAKMaetcvvrekQDYKQKLKALRIEVnklkEDLNEKTTENNEQreeIIRLKQEKSCLHDELi 297
Cdd:COG3206 255 ALPE----------LLQSPVI---------QQLRAQLAELEAEL----AELSARYTPNHPD---VIALRAQIAALRAQL- 307
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1039770978 298 ftverEKRKDELLDIAKSKQDRTNSELQNLRQIYVKQQSDLQFLNfniESSQELIQI 354
Cdd:COG3206 308 -----QQEAQRILASLEAELEALQAREASLQAQLAQLEARLAELP---ELEAELRRL 356
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
83-286 |
4.61e-03 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 40.49 E-value: 4.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770978 83 DKELNDM-VAVHQRQLLSWEEDrQKVLTLEERCSKLEGELHKRTDIIKSLMKKVKTLESNQAECQTALQKTQQQLQEMAQ 161
Cdd:pfam15921 596 EKEINDRrLELQEFKILKDKKD-AKIRELEARVSDLELEKVKLVNAGSERLRAVKDIKQERDQLLNEVKTSRNELNSLSE 674
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770978 162 KathSTLLSEDLEARNENLSSTLVDLSAQVGQLQAR-EQALTTMIKLKDKD-------------IIEAVNHISDCSGKFK 227
Cdd:pfam15921 675 D---YEVLKRNFRNKSEEMETTTNKLKMQLKSAQSElEQTRNTLKSMEGSDghamkvamgmqkqITAKRGQIDALQSKIQ 751
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1039770978 228 LLEHALRDAKMAETCVVREKQDYKQKLKALRIEVNKLKEDLNEKTTENNEQREEIIRLK 286
Cdd:pfam15921 752 FLEEAMTNANKEKHFLKEEKNKLSQELSTVATEKNKMAGELEVLRSQERRLKEKVANME 810
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
61-334 |
5.08e-03 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 39.88 E-value: 5.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770978 61 ETSTIEKQRKELQLLIGELKDRDKELNDMVAVHQRQLLSWEEDRQkvlTLEERCSKLEGELHKRTDIIKSLMKKVKTLES 140
Cdd:pfam07888 95 KHEELEEKYKELSASSEELSEEKDALLAQRAAHEARIRELEEDIK---TLTQRVLERETELERMKERAKKAGAQRKEEEA 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770978 141 NQAECQTALQKTQQQLQEM-----------AQKATHSTLLSEDL-------------EARNEnlsSTLVDLSAQVGQLQA 196
Cdd:pfam07888 172 ERKQLQAKLQQTEEELRSLskefqelrnslAQRDTQVLQLQDTIttltqklttahrkEAENE---ALLEELRSLQERLNA 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770978 197 REQA-------LTTMIKLKDKDIIE---AVNHISDCSGKFKLLEHALRDAK----MAETCVVREKQDYKQKLKALRIEVN 262
Cdd:pfam07888 249 SERKveglgeeLSSMAAQRDRTQAElhqARLQAAQLTLQLADASLALREGRarwaQERETLQQSAEADKDRIEKLSAELQ 328
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039770978 263 KLKEDLNEKTTENNEQREEiirLKQEKSClhdELIFTVEREKRKDEL---LDIAKSKQDRTNSELQNLRQiYVKQ 334
Cdd:pfam07888 329 RLEERLQEERMEREKLEVE---LGREKDC---NRVQLSESRRELQELkasLRVAQKEKEQLQAEKQELLE-YIRQ 396
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
71-339 |
5.32e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 40.33 E-value: 5.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770978 71 ELQLLIGELKDRDKELNDMVAVHQRQllsweedRQKVLTLEERCSKLEgELHKRTDIIK--SLMKKVKTLESNQAECQTA 148
Cdd:PRK04863 838 ELRQLNRRRVELERALADHESQEQQQ-------RSQLEQAKEGLSALN-RLLPRLNLLAdeTLADRVEEIREQLDEAEEA 909
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770978 149 LQKTQQQLQEMAQKATHSTLLSEDlEARNENLSSTLVDLSAQVGQLQAREQALTTMIK----LKDKDIIEAVNHISDCS- 223
Cdd:PRK04863 910 KRFVQQHGNALAQLEPIVSVLQSD-PEQFEQLKQDYQQAQQTQRDAKQQAFALTEVVQrrahFSYEDAAEMLAKNSDLNe 988
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770978 224 ---GKFKLLEHALRDAKMAETCVVREKQDYKQ---KLK----ALRIEVNKLKEDLNEKTTENNEQREEIIRLKQEKscLH 293
Cdd:PRK04863 989 klrQRLEQAEQERTRAREQLRQAQAQLAQYNQvlaSLKssydAKRQMLQELKQELQDLGVPADSGAEERARARRDE--LH 1066
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1039770978 294 DELIftvEREKRKDELLdiakSKQDRTNSELQNLRQIYVKQQSDLQ 339
Cdd:PRK04863 1067 ARLS---ANRSRRNQLE----KQLTFCEAEMDNLTKKLRKLERDYH 1105
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
52-366 |
6.37e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 39.75 E-value: 6.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770978 52 RRQNIGSEVETSTIEKQRKELQLLIGELKDRDKELNDMVAVHQRQLLSWEEDRQKVLTLEERCSKLEGELHKRTDI---- 127
Cdd:COG4717 110 ELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQlsla 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770978 128 ----IKSLMKKVKTLESNQAECQTALQKTQQQLQEMAQK--ATHSTLLSEDLEARNENLSSTLVDLSAQVGQLQAREQAL 201
Cdd:COG4717 190 teeeLQDLAEELEELQQRLAELEEELEEAQEELEELEEEleQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLL 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770978 202 TTMIKLkdKDIIEAVNHISDCSGKFKLLEHALRDAKMAETCVVREKQDYKQ-KLKALRIEVNKLKEDLNEKTTENNEQRE 280
Cdd:COG4717 270 SLILTI--AGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEeELEELLAALGLPPDLSPEELLELLDRIE 347
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770978 281 EIIRLKQEKSCLHDELIfTVEREKRKDELLDIAKSKQDRTNSELQNLRQIYVKQQSDLQFLNFNIESSQELIQiHGLKME 360
Cdd:COG4717 348 ELQELLREAEELEEELQ-LEELEQEIAALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELE-ELLEAL 425
|
....*.
gi 1039770978 361 EPKALE 366
Cdd:COG4717 426 DEEELE 431
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
59-361 |
6.75e-03 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 39.68 E-value: 6.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770978 59 EVETSTIEKQRKELQLLIGELKDRdKELNDMVAvhQRQLLSWEEDRQKVL-TLEERCSKLEGE-LHKRTDIIKSLMKKVK 136
Cdd:COG5022 786 LVDYELKWRLFIKLQPLLSLLGSR-KEYRSYLA--CIIKLQKTIKREKKLrETEEVEFSLKAEvLIQKFGRSLKAKKRFS 862
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770978 137 TL--ESNQAECQTALQKTQQQLQEMAQKATHSTLLSEdleaRNENLSSTLVDLSAQVgqlqareqalttmiklkDKDIIE 214
Cdd:COG5022 863 LLkkETIYLQSAQRVELAERQLQELKIDVKSISSLKL----VNLELESEIIELKKSL-----------------SSDLIE 921
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770978 215 AVNHISDCSGKFK--LLEHALRDAKMAETCVVREKQDYKQKLKALRiEVNKLKEDLNEKTT----ENNEQREEIIRLKQE 288
Cdd:COG5022 922 NLEFKTELIARLKklLNNIDLEEGPSIEYVKLPELNKLHEVESKLK-ETSEEYEDLLKKSTilvrEGNKANSELKNFKKE 1000
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039770978 289 KSCLHDELIFTVEREKRKDELldiakskqDRTNSELQNLRQIYVKQQSDLQFLNfnieSSQELIQIHGLKMEE 361
Cdd:COG5022 1001 LAELSKQYGALQESTKQLKEL--------PVEVAELQSASKIISSESTELSILK----PLQKLKGLLLLENNQ 1061
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
126-215 |
7.11e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 39.43 E-value: 7.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039770978 126 DIIKSLMKKVKTLESNQAECQTALQKTQQQLQEMAQKAthstllsEDLEARNENLSSTLVDLSAQVGQLQAREQALTTMI 205
Cdd:COG3883 133 DLLEELKADKAELEAKKAELEAKLAELEALKAELEAAK-------AELEAQQAEQEALLAQLSAEEAAAEAQLAELEAEL 205
|
90
....*....|
gi 1039770978 206 KLKDKDIIEA 215
Cdd:COG3883 206 AAAEAAAAAA 215
|
|
| |
